Structural comparison of 26S rRNA-binding ribosomal protein L25 from two different yeast strains and the equivalent proteins from three eubacteria and two chloroplasts

• Published in: Journal of molecular evolution Vol. 28; no. 5; p. 418
• Main Authors: Raué, H A, Otaka, E, Suzuki, K
• Format: Journal Article
• Language: English
• Published: Germany 01.05.1989
• Subjects: Amino Acid Sequence; Bacterial Proteins - genetics; Biological Evolution; Candida - genetics; Chloroplasts; Escherichia coli - genetics; Fungal Proteins - genetics; Geobacillus stearothermophilus - genetics; Molecular Sequence Data; Molecular Structure; Mycoplasma - genetics; Nicotiana - genetics; Plants - genetics; Plants, Toxic; Ribosomal Proteins - genetics; Saccharomyces - genetics; Sequence Homology, Nucleic Acid; Species Specificity
• ISSN: 0022-2844
• DOI: 10.1007/BF02603077

The sequences of Saccharomyces carlsbergensis ribosomal protein (r-protein) SL25* and its equivalents from Candida utilis (CL25), Escherichia coli (EL23), Bacillus stearothermophilus (BL23), Mycoplasma capricolum (ML23), Marchantia polymorpha chloroplasts (McpL23), and Nicotiana tabacum chloroplasts (NcpL23) were examined using a computer program that evaluates the extent of sequence similarity by calculating correlation coefficients for each pair of residues in two proteins from a number of physical properties of individual amino acids. Comparison matrices demonstrate that the prokaryotic sequences (including McpL23 and NcpL23) can be aligned unambiguously by introducing small internal deletions/insertions at three specific positions. A similar comparison brought to light a clear evolutionary relationship between the prokaryotic and the yeast proteins despite the fact that visual inspection of these sequences revealed only limited similarity. The alignment deduced from this comparison shows the two yeast r-proteins to have acquired a long (50-60 amino acids) N-terminal extension as well as a 13-amino acid-long deletion near the C-terminus. The significance of these findings in terms of the evolution of r-proteins in general and the biological function of various parts of the SL25 protein in particular is discussed.